PBL34_ARATH
ID PBL34_ARATH Reviewed; 493 AA.
AC Q9LFP7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine/threonine-protein kinase PBL34 {ECO:0000303|PubMed:29907700};
DE EC=2.7.11.1 {ECO:0000269|PubMed:31922267};
DE AltName: Full=PBS1-like protein 34 {ECO:0000303|PubMed:29907700};
DE AltName: Full=Receptor-like cytoplasmic kinase PBL34 {ECO:0000303|PubMed:29907700};
GN Name=PBL34 {ECO:0000303|PubMed:29907700};
GN Synonyms=PIX7 {ECO:0000303|PubMed:23951354};
GN OrderedLocusNames=At5g15080 {ECO:0000312|EMBL:AED92114.1};
GN ORFNames=F2G14.200 {ECO:0000312|EMBL:CAC01827.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
RN [5]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=29907700; DOI=10.1104/pp.18.00486;
RA Rao S., Zhou Z., Miao P., Bi G., Hu M., Wu Y., Feng F., Zhang X.,
RA Zhou J.M.;
RT "Roles of receptor-like cytoplasmic kinase VII members in pattern-triggered
RT immune signaling.";
RL Plant Physiol. 177:1679-1690(2018).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SD129, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT THR-306 AND THR-310, AND MUTAGENESIS OF LYS-180.
RX PubMed=31922267; DOI=10.15252/embj.2019102856;
RA Luo X., Wu W., Liang Y., Xu N., Wang Z., Zou H., Liu J.;
RT "Tyrosine phosphorylation of the lectin receptor-like kinase LORE regulates
RT plant immunity.";
RL EMBO J. 39:e102856-e102856(2020).
CC -!- FUNCTION: Involved in chitin-triggered immune signaling and is required
CC for reactive oxygen species (ROS) production (PubMed:29907700). Acts
CC downstream of SD129 in defense signaling triggered by the pathogen-
CC associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-
CC hydroxy fatty acid (PubMed:31922267). {ECO:0000269|PubMed:29907700,
CC ECO:0000269|PubMed:31922267}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:31922267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:31922267};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:31922267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:31922267};
CC -!- SUBUNIT: Interacts with the Xanthomonas campestris effector XopAC/AvrAC
CC (PubMed:23951354). Interacts with SD129 (PubMed:31922267).
CC {ECO:0000269|PubMed:23951354, ECO:0000269|PubMed:31922267}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31922267};
CC Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
CC -!- PTM: Phosphorylated by SD129 at Thr-306 and Thr-310 in response to the
CC pathogen-associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain
CC 3-hydroxy fatty acid. {ECO:0000269|PubMed:31922267}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-55 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AL391146; CAC01827.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92114.1; -; Genomic_DNA.
DR EMBL; AY062520; AAL32598.1; -; mRNA.
DR EMBL; BT002577; AAO00937.1; -; mRNA.
DR PIR; T51453; T51453.
DR RefSeq; NP_197012.1; NM_121512.5.
DR AlphaFoldDB; Q9LFP7; -.
DR SMR; Q9LFP7; -.
DR BioGRID; 16637; 3.
DR IntAct; Q9LFP7; 2.
DR STRING; 3702.AT5G15080.1; -.
DR iPTMnet; Q9LFP7; -.
DR PaxDb; Q9LFP7; -.
DR PRIDE; Q9LFP7; -.
DR ProteomicsDB; 235031; -.
DR EnsemblPlants; AT5G15080.1; AT5G15080.1; AT5G15080.
DR GeneID; 831360; -.
DR Gramene; AT5G15080.1; AT5G15080.1; AT5G15080.
DR KEGG; ath:AT5G15080; -.
DR Araport; AT5G15080; -.
DR TAIR; locus:2147805; AT5G15080.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; Q9LFP7; -.
DR OMA; YEAKSAT; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LFP7; -.
DR PRO; PR:Q9LFP7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFP7; baseline and differential.
DR Genevisible; Q9LFP7; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..493
FT /note="Serine/threonine-protein kinase PBL34"
FT /id="PRO_0000401337"
FT DOMAIN 142..428
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 148..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 225
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31922267"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31922267"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT MUTAGEN 180
FT /note="K->E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:31922267"
SQ SEQUENCE 493 AA; 54799 MW; 9BF1B80EF28B960C CRC64;
MGLDAVKAKG NWKSEKPKET ENKNHKKKNG DDNKSRNEEE EEGEASGCWV KFRFMIGCIP
SKSDLDASSS SIYGSNCTVT TMESKSANEK SNDQPVGQVS STTTTSNAES SSSTPVISEE
LNISSHLRKF TFNDLKLSTR NFRPESLLGE GGFGCVFKGW IEENGTAPVK PGTGLTVAVK
TLNPDGLQGH KEWLAEINFL GNLLHPNLVK LVGYCIEDDQ RLLVYEFMPR GSLENHLFRR
SLPLPWSIRM KIALGAAKGL SFLHEEALKP VIYRDFKTSN ILLDADYNAK LSDFGLAKDA
PDEGKTHVST RVMGTYGYAA PEYVMTGHLT SKSDVYSFGV VLLEMLTGRR SMDKNRPNGE
HNLVEWARPH LLDKRRFYRL LDPRLEGHFS IKGAQKVTQL AAQCLSRDPK IRPKMSDVVE
ALKPLPHLKD MASSSYYFQT MQAERLKNGS GRSQGFGSRN GQHQPVFRTL SSPHGSSPYR
HQIPSPKPKG ATT
